Additional information
| Qty | 100 μg, 500 μg, 1 mg |
|---|---|
| Shipping in Dry Ice | yes |
S100A8-A9 - heterodimer
1.160,00€ – 3.700,00€
Human, recombinant
Heterodimer complex of S100A8 and S100A9 (Calprotectin)
CAT # G02S1A89
| Catalog n. | Qty | Price |
|---|---|---|
| 1.160,00€ | ||
| 2.600,00€ | ||
| 3.700,00€ | ||
| VAT not included | ||
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Description
Description
Recombinant heterodimer complex of S100A8 and S100A9 (Calprotectin). The heterodimer consists of the recombinant S100A8 C42S mutant (residues 1-93, UniProtKB accession P05109) and S100A9 C3S mutant (residues 1-114, UniProtKB accession P06702). Both proteins were separately cloned from human cDNA and expressed in E. coli.
Recombinant heterodimer complex of S100A8 and S100A9 (Calprotectin). The heterodimer consists of the recombinant S100A8 C42S mutant (residues 1-93, UniProtKB accession P05109) and S100A9 C3S mutant (residues 1-114, UniProtKB accession P06702). Both proteins were separately cloned from human cDNA and expressed in E. coli.
Purity
> 95% by SDS-PAGE. The complex is observed, in denaturing conditions, as two bands migrating at a molecular weight below 14.4 kDa.
> 95% by SDS-PAGE. The complex is observed, in denaturing conditions, as two bands migrating at a molecular weight below 14.4 kDa.
Supplied as
1 mg/mL solution in Tris 20 mM, pH 7.5, EDTA 1 mM, NaCl 100 mM. The concentration is calculated by the analysis of the absorbance at 280 nm (ε280 = 11460 M-1cm-1 calculated).
1 mg/mL solution in Tris 20 mM, pH 7.5, EDTA 1 mM, NaCl 100 mM. The concentration is calculated by the analysis of the absorbance at 280 nm (ε280 = 11460 M-1cm-1 calculated).
Storage
-20°C. The protein is stable at 4°C for at least 2 weeks and at 25°C for several hours. After initial defrost, aliquot the product into individual tubes and refreeze at -20°C. Avoid repeated freeze/thaw cycles.
-20°C. The protein is stable at 4°C for at least 2 weeks and at 25°C for several hours. After initial defrost, aliquot the product into individual tubes and refreeze at -20°C. Avoid repeated freeze/thaw cycles.
References
Korndörfer, I.P., Brueckner, F. & Skerra, A. J. Mol. Biol. 370 (5), 887-898 (2007).
Ikemoto, M. et al. Clin. Chim. Acta 376 (1-2), 197-204 (2007).
Nacken, W. & Kerkhoff, C. FEBS Lett. 581 (26), 5127-5130 (2007).
Vogl, T. et al. Biochim. Biophys. Acta – Mol. Cell Res. 1763 (11), 1298-1306 (2006).
Korndörfer, I.P., Brueckner, F. & Skerra, A. J. Mol. Biol. 370 (5), 887-898 (2007).
Ikemoto, M. et al. Clin. Chim. Acta 376 (1-2), 197-204 (2007).
Nacken, W. & Kerkhoff, C. FEBS Lett. 581 (26), 5127-5130 (2007).
Vogl, T. et al. Biochim. Biophys. Acta – Mol. Cell Res. 1763 (11), 1298-1306 (2006).